ID D9XIU8_STRVT Unreviewed; 569 AA.
AC D9XIU8;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 11-DEC-2019, entry version 64.
DE RecName: Full=Urease subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
DE EC=3.5.1.5 {ECO:0000256|HAMAP-Rule:MF_01953};
DE AltName: Full=Urea amidohydrolase subunit alpha {ECO:0000256|HAMAP-Rule:MF_01953};
GN Name=ureC {ECO:0000256|HAMAP-Rule:MF_01953};
GN ORFNames=SSQG_05581 {ECO:0000313|EMBL:EFL35063.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=591159 {ECO:0000313|EMBL:EFL35063.1, ECO:0000313|Proteomes:UP000004184};
RN [1] {ECO:0000313|EMBL:EFL35063.1, ECO:0000313|Proteomes:UP000004184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494
RC {ECO:0000313|Proteomes:UP000004184};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
CC ECO:0000256|SAAS:SAAS01119912};
CC -!- COFACTOR:
CC Name=Ni cation; Xref=ChEBI:CHEBI:25516;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01953,
CC ECO:0000256|PIRSR:PIRSR611612-51};
CC Note=Binds 2 nickel ions per subunit. {ECO:0000256|HAMAP-Rule:MF_01953,
CC ECO:0000256|PIRSR:PIRSR611612-51};
CC -!- PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from
CC urea (urease route): step 1/1. {ECO:0000256|HAMAP-Rule:MF_01953,
CC ECO:0000256|SAAS:SAAS00317636}.
CC -!- SUBUNIT: May form a heterohexamer of 3 UreC (alpha) and 3 UreAB
CC (gamma/beta) subunits. May also form a heterotrimer of UreA (gamma),
CC UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to
CC form the active enzyme. {ECO:0000256|HAMAP-Rule:MF_01953}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953,
CC ECO:0000256|PROSITE-ProRule:PRU00700, ECO:0000256|SAAS:SAAS00548017}.
CC -!- PTM: Carbamylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000256|PIRSR:PIRSR611612-50}.
CC -!- PTM: Carboxylation allows a single lysine to coordinate two nickel
CC ions. {ECO:0000256|HAMAP-Rule:MF_01953}.
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Urease alpha subunit family. {ECO:0000256|HAMAP-Rule:MF_01953,
CC ECO:0000256|RuleBase:RU004158, ECO:0000256|SAAS:SAAS00849550}.
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DR EMBL; GG657757; EFL35063.1; -; Genomic_DNA.
DR RefSeq; WP_003993166.1; NZ_GG657757.1.
DR STRING; 591159.ACEZ01000170_gene3599; -.
DR EnsemblBacteria; EFL35063; EFL35063; SSQG_05581.
DR GeneID; 34225735; -.
DR eggNOG; ENOG4105CQM; Bacteria.
DR eggNOG; COG0804; LUCA.
DR OrthoDB; 157757at2; -.
DR UniPathway; UPA00258; UER00370.
DR Proteomes; UP000004184; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009039; F:urease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043419; P:urea catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.30.40.10; -; 1.
DR HAMAP; MF_01953; Urease_alpha; 1.
DR InterPro; IPR006680; Amidohydro-rel.
DR InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR011612; Urease_alpha_N_dom.
DR InterPro; IPR005848; Urease_asu.
DR InterPro; IPR017951; Urease_asu_c.
DR InterPro; IPR029754; Urease_Ni-bd.
DR Pfam; PF01979; Amidohydro_1; 1.
DR Pfam; PF00449; Urease_alpha; 1.
DR PRINTS; PR01752; UREASE.
DR SUPFAM; SSF51338; SSF51338; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR PROSITE; PS01120; UREASE_1; 1.
DR PROSITE; PS51368; UREASE_3; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW ProRule:PRU00700, ECO:0000256|SAAS:SAAS00317631};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PROSITE-
KW ProRule:PRU00700, ECO:0000256|SAAS:SAAS00321417};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01953,
KW ECO:0000256|PIRSR:PIRSR611612-51, ECO:0000256|SAAS:SAAS00321440};
KW Nickel {ECO:0000256|HAMAP-Rule:MF_01953, ECO:0000256|PIRSR:PIRSR611612-51,
KW ECO:0000256|SAAS:SAAS00317628}.
FT DOMAIN 140..569
FT /note="Urease"
FT /evidence="ECO:0000259|PROSITE:PS51368"
FT ACT_SITE 328
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-52, ECO:0000256|PROSITE-
FT ProRule:PRU00700"
FT METAL 145
FT /note="Nickel 1; via tele nitrogen"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT METAL 147
FT /note="Nickel 1; via tele nitrogen"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT METAL 225
FT /note="Nickel 1; via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT METAL 225
FT /note="Nickel 2; via carbamate group"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT METAL 254
FT /note="Nickel 2; via pros nitrogen"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT METAL 280
FT /note="Nickel 2; via tele nitrogen"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT METAL 368
FT /note="Nickel 1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-51"
FT BINDING 227
FT /note="Substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PROSITE-ProRule:PRU00700"
FT MOD_RES 225
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01953,
FT ECO:0000256|PIRSR:PIRSR611612-50"
SQ SEQUENCE 569 AA; 59776 MW; 12765E3D44BEEC1C CRC64;
MSRPGGHPAE ARRLTPYEYA ATHGPRAGDR VRLGDSGLVV KVESDSQRPG DEFLAGFGKT
ARDGMHLRAA AVRETCDAVI SNVVVIDAAQ GVRKVSIGIR EGRICSIGRA GNPDTLDGVD
VVVGTGTSIY SGEGLIATAG AVDTHVHLLS PRVMEASLAS GVTTIIGQEF GPVWGVGVNS
PWALRHAFSA FDAWPVNIGF LGRGSSSHAA PLVEALAEGG ACGFKVHEDM GAHTRALDTA
LRVAEEHDVQ VALHSDGLNE CLSVEDTLRV LEGRTIHAFH IEGCGGGHVP NVLKMAGVPN
VIGSSTNPTL PFGRDAVAEH YGMIVSVHDL KTDLPGDAAM ARDRIRAGTM GAEDVLHDLG
AIGITSSDAQ GMGRAGETVR RTFAMAGKMK TEFGAPDEHD NDRVLRYMAK LTINPALAHG
LAHEVGSLEV GKLADIVLWR PEYFGAKPQL VLKSGFPAYG VTGDPNAATD TCEPLVLGPQ
FGAHGGTPAD ISVAFVAQAA LDQGRDGMPT RRRRVAVRGT RGIGPADLRL NSRTGAVDVD
QRTGLVTLDG EPLRSEPAES VSLNRLYFL
//
